PEPTIDYLPROLYL ISOMERASE FROM E. COLI
The structure was published by Edwards, K.J., Ollis, D.L., and Dixon, N.E., in 1997 in a paper entitled "Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1996.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of PEPTIDYLPROLYL ISOMERASE. This molecule has the UniProt identifier P23869 (PPIB_ECOLI). The sample contained 164 residues which is 100% of the natural sequence. Out of 164 residues 157 were observed and are deposited in the PDB.
The molecule most likely forms homodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: